YSL1_ARATH
ID YSL1_ARATH Reviewed; 673 AA.
AC Q6R3L0; O22979; Q94EY9; Q9SU45;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Metal-nicotianamine transporter YSL1;
DE AltName: Full=Protein YELLOW STRIPE LIKE 1;
DE Short=AtYSL1;
GN Name=YSL1; OrderedLocusNames=At4g24120; ORFNames=T19F6.110, T19F6.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Roberts L.A., Walker E.L.;
RT "The yellow stripe-like (YSL) family of metal-nicotianamine transporters.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-673.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11201743; DOI=10.1038/35053080;
RA Curie C., Panaviene Z., Loulergue C., Dellaporta S.L., Briat J.-F.,
RA Walker E.L.;
RT "Maize yellow stripe1 encodes a membrane protein directly involved in
RT Fe(III) uptake.";
RL Nature 409:346-349(2001).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=13129917; DOI=10.1074/jbc.m309338200;
RA Wintz H., Fox T., Wu Y.-Y., Feng V., Chen W., Chang H.-S., Zhu T.,
RA Vulpe C.D.;
RT "Expression profiles of Arabidopsis thaliana in mineral deficiencies reveal
RT novel transporters involved in metal homeostasis.";
RL J. Biol. Chem. 278:47644-47653(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16297069; DOI=10.1111/j.1365-313x.2005.02569.x;
RA Le Jean M., Schikora A., Mari S., Briat J.-F., Curie C.;
RT "A loss-of-function mutation in AtYSL1 reveals its role in iron and
RT nicotianamine seed loading.";
RL Plant J. 44:769-782(2005).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=16815956; DOI=10.1104/pp.106.082586;
RA Waters B.M., Chu H.-H., DiDonato R.J. Jr., Roberts L.A., Eisley R.B.,
RA Lahner B., Salt D.E., Walker E.L.;
RT "Mutations in Arabidopsis yellow stripe-like1 and yellow stripe-like3
RT reveal their roles in metal ion homeostasis and loading of metal ions in
RT seeds.";
RL Plant Physiol. 141:1446-1458(2006).
CC -!- FUNCTION: Involved in iron loading of the seeds. Acts probably as a
CC transporter of iron- and metal-nicotianamine chelates.
CC {ECO:0000269|PubMed:16297069, ECO:0000269|PubMed:16815956}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Low levels of expression in leaves and shoots, but
CC not detected in roots. Restricted to the vasculature, in the xylem
CC parenchyma surrounding xylem tubes. Expressed in pollen grains, in the
CC vasculature of petals and sepals, in the carpel veins, in the style
CC underneath the stigmatic papillae, in the vascular tissue of the
CC funiculus and in the chalazal endosperm. {ECO:0000269|PubMed:13129917,
CC ECO:0000269|PubMed:16297069, ECO:0000269|PubMed:16815956}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during leaf senescence.
CC {ECO:0000269|PubMed:16815956}.
CC -!- INDUCTION: Slight induction by manganese, copper or zinc deficiency.
CC Inhibited upon iron deficiency and induced by iron overload.
CC {ECO:0000269|PubMed:13129917, ECO:0000269|PubMed:16297069,
CC ECO:0000269|PubMed:16815956}.
CC -!- DISRUPTION PHENOTYPE: Plants do not show visible phenotype, but a
CC decreased iron and nicotianamine content in seeds resulting in a
CC transient defect in germination. {ECO:0000269|PubMed:16297069,
CC ECO:0000269|PubMed:16815956}.
CC -!- SIMILARITY: Belongs to the YSL (TC 2.A.67.2) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK62460.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY515560; AAS00691.1; -; mRNA.
DR EMBL; AC002343; AAB63613.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109619; CAB51655.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161560; CAB81330.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84852.1; -; Genomic_DNA.
DR EMBL; AF387015; AAK62460.1; ALT_INIT; mRNA.
DR PIR; T13460; T13460.
DR RefSeq; NP_567694.2; NM_118544.4.
DR AlphaFoldDB; Q6R3L0; -.
DR SMR; Q6R3L0; -.
DR STRING; 3702.AT4G24120.1; -.
DR TCDB; 2.A.67.2.2; the oligopeptide transporter (opt) family.
DR iPTMnet; Q6R3L0; -.
DR PaxDb; Q6R3L0; -.
DR PRIDE; Q6R3L0; -.
DR ProteomicsDB; 242373; -.
DR EnsemblPlants; AT4G24120.1; AT4G24120.1; AT4G24120.
DR GeneID; 828512; -.
DR Gramene; AT4G24120.1; AT4G24120.1; AT4G24120.
DR KEGG; ath:AT4G24120; -.
DR Araport; AT4G24120; -.
DR TAIR; locus:2134956; AT4G24120.
DR eggNOG; ENOG502QSSI; Eukaryota.
DR HOGENOM; CLU_015477_2_0_1; -.
DR InParanoid; Q6R3L0; -.
DR OMA; WPGVMVM; -.
DR OrthoDB; 525938at2759; -.
DR PhylomeDB; Q6R3L0; -.
DR PRO; PR:Q6R3L0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6R3L0; baseline and differential.
DR Genevisible; Q6R3L0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0051980; F:iron-nicotianamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0003006; P:developmental process involved in reproduction; IGI:TAIR.
DR GO; GO:0010039; P:response to iron ion; IEP:TAIR.
DR GO; GO:0048316; P:seed development; IGI:TAIR.
DR InterPro; IPR004813; OPT.
DR InterPro; IPR045035; YSL-like.
DR PANTHER; PTHR31645; PTHR31645; 1.
DR Pfam; PF03169; OPT; 1.
DR TIGRFAMs; TIGR00728; OPT_sfam; 1.
PE 2: Evidence at transcript level;
KW Ion transport; Iron; Iron transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..673
FT /note="Metal-nicotianamine transporter YSL1"
FT /id="PRO_0000311412"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 72
FT /note="T -> A (in Ref. 1; AAS00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> G (in Ref. 1; AAS00691)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="Q -> R (in Ref. 2; AAB63613 and 4; AAK62460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 74392 MW; C9667829E9D388B9 CRC64;
MEIEQRRIMK REGEEEEDNN QLSLQEEEPD TEEEMSGRTI EPWTKQITVR GVFVSIVIGV
VFSVIAQKLN LTTGIVPNLN SSAALLAFVF VQTWTKILKK SGFVAKPFTR QENTMIQTSA
VACYGIAVGG GFASYLLGLN HKTYVLSGVN LEGNSPKSVK EPGLGWMTAY LFVVCFIGLF
VLIPLRKVMI VDLKLTYPSG LATAVLINGF HTQGDAQAKK QVRGFMKYFS FSFLWGFFQW
FFSGIEDCGF AQFPTFGLKA WKQTFFFDFS MTFVGAGMIC SHLVNLSLLL GAILSYGLMW
PLLDKLKGSW FPDNLDEHNM KSIYGYKVFL SVALILGDGL YTFVKILFVT IANVNARLKN
KPNDLDDVGH KKQRKDLKED ENFLRDKIPM WFAVSGYLTF AAVSTVVVPL IFPQLKWYYV
IVAYIFAPSL AFCNAYGAGL TDINMAYNYG KIGLFVIAAV TGRENGVVAG LAGCGLIKSV
VSVSCILMQD FKTAHYTMTS PKAMFASQMI GTVVGCIVTP LSFFLFYKAF DIGNPNGEFK
APYALIYRNM AILGVQGFSA LPLHCLQMCY GFFGFAVLVN VVRDLTPAKI GRFMPLPTAM
AVPFLVGAYF AIDMCVGTLI VFVWEKMNRK KAEFMVPAVA SGLICGEGLW TLPAAVLALA
GVKPPICMKF LAS
